Four Forces that Stabilize a Protein’s Structure at the Tertiary Level
There are several types of bonds and forces that hold a protein in its tertiary structure. Hydrophobic interactions contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will search for interactions with water, while amino acids with hydrophobic "R" groups will avoid water and clump towards the center protein. Hydrogen bonding in the polypeptide chain and between amino acid "R" groups helps to stabilize protein structure by holding the protein in the shape made by the hydrophobic interactions. Due to protein folding, ionic bonding can occur between the positively and negatively charged "R" groups that come in contact with one another. Folding can also result in covalent bonding between the "R" groups of cysteine amino acids, also known as a disulfide bridge (strongest bond). Van der Waals forces interactions help in the stabilization of protein structure. These interactions refer to to the attractive and repulsive forces that occur between molecules that become polarized. These forces contribute to the bonding that occurs between molecules. (Borges,2014)

Bovine Spongiform Encephalopathy
Mad cow disease or bovine spongiform encephalopathy is a deadly neurological disease that affects adult cattle. It is transmitted from animal to animal through contaminated food that contain infected central nervous system and spinal cord remnants. The contaminated food contain prions, a type of misfolded protein. A healthy brain prion protein (PrP) Is converted into a diseased PrPSc. “All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. Amyloid aggregates are fibrils, growing at their ends, and replicate when breakage causes two growing ends to become four growing ends.” (Mansel, 1999) The disease proteins continue their attack on the central nervous system and spinal cord until death. (Thompson, 2014)

Chaperone Protein in BSE
Chaperone protein can be described as “helper molecules.” These helper molecules aid proteins in finding their correct configuration and function. However, chaperone proteins cannot assist prions. Prions act as their own chaperone. Prions attach to a normal protein and cause them to change into a prion. (Thompson, 2012)

Decrease Risk of transmitting Prions
The food regulation industries can decrease the transmission of prions by testing adult bovine and sheep. Recalls can be instituted for possibly contaminated food. Companies can avoid processing any part of the central nervous system and spinal cord of bovine to keep them from entering the food supply.

References

Borges, K. (2014) Bonds that stabilize protein tertiary structure. Retrieved from https://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=b8686074-1a41-428c-ab18-037fa5e070e3
Helmenstine, A.M. Mad Cow Disease: What You Need to Know About Bovine Spongiform Encephalopathy. Retrieve from http://chemistry.about.com/cs/howthingswork/a/aa122703a.htm Hudon-Miller, S. (2012) Dehydration and hydrolysis. Retrieved from https://wgu.hosted.panopto.com/Panopto/Pages/Viewer/Default.aspx?id=b78d41cc-a691-49ff-a315- SL, Cotran RS, Kumar V et al., eds. (1999). Robbins pathologic basis of disease. Philadelphia: Saunders7.
St. Rosemary Educational Institution. "Protein Structures: Primary, Secondary, Tertiary, Quaternary." http://schoolworkhelper.net/. St. Rosemary Educational Institution, Last Update: 2015. Web. Retrieved on: Sunday 23rd August 2015. http://schoolworkhelper.net/protein-structures-primary-secondary-tertiary-quaternary/ Thompson, J. (2014) BSE. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=3c62aca1-68ff-4033-9f02-f07a86bb3cfc
Masel J, Jansen VA, Nowak MA (Mar 1999). "Quantifying the kinetic parameters of prion replication". Biophysical Chemistry 77 (2-3): 139–52. Retrieved from https://en.wikipedia.org/wiki/Prion#cite_note-Masel_99-6